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Conserved domains on  [gi|167234437|ref|NP_001107834|]
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echinoderm microtubule-associated protein-like 4 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 170-238 4.45e-36

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


:

Pssm-ID: 460922  Cd Length: 72  Bit Score: 130.36  E-value: 4.45e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167234437  170 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 238
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 6.42e-31

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


:

Pssm-ID: 409271  Cd Length: 59  Bit Score: 115.47  E-value: 6.42e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167234437   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950    1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 445-805 2.57e-26

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 109.73  E-value: 2.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 445 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 524
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 525 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 598
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 599 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 669
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 670 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 749
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167234437 750 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 805
Cdd:cd00200  238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 245-598 1.36e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 90.09  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 245 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 325 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 401
Cdd:cd00200   70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 402 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 480
Cdd:cd00200  139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 481 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 560
Cdd:cd00200  207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 167234437 561 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 598
Cdd:cd00200  246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 170-238 4.45e-36

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


Pssm-ID: 460922  Cd Length: 72  Bit Score: 130.36  E-value: 4.45e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167234437  170 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 238
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 6.42e-31

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


Pssm-ID: 409271  Cd Length: 59  Bit Score: 115.47  E-value: 6.42e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167234437   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950    1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 445-805 2.57e-26

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 109.73  E-value: 2.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 445 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 524
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 525 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 598
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 599 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 669
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 670 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 749
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167234437 750 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 805
Cdd:cd00200  238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
442-806 1.33e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.39  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 442 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 518
Cdd:COG2319   69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 519 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 596
Cdd:COG2319  146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 597 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 676
Cdd:COG2319  226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 677 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 756
Cdd:COG2319  302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 167234437 757 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 806
Cdd:COG2319  356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 245-598 1.36e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.09  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 245 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 325 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 401
Cdd:cd00200   70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 402 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 480
Cdd:cd00200  139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 481 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 560
Cdd:cd00200  207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 167234437 561 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 598
Cdd:cd00200  246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 COG2319
WD40 repeat [General function prediction only];
229-479 2.96e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.72  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 229 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 302
Cdd:COG2319  176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 303 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 380
Cdd:COG2319  244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 381 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 459
Cdd:COG2319  319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                        250       260
                 ....*....|....*....|
gi 167234437 460 MRNGMLLTGGGKDRKIILWD 479
Cdd:COG2319  381 SPDGRTLASGSADGTVRLWD 400
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 659-691 2.15e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.60  E-value: 2.15e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 167234437   659 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 691
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
657-691 3.63e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 167234437  657 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 691
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 631-694 4.07e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.70  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167234437 631 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 694
Cdd:PTZ00420  89 ILASGSEDLTIRVWEIPHNDEsvKEIKDPQCilKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIEN 157
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 170-238 4.45e-36

HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.


Pssm-ID: 460922  Cd Length: 72  Bit Score: 130.36  E-value: 4.45e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167234437  170 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 238
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 6.42e-31

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


Pssm-ID: 409271  Cd Length: 59  Bit Score: 115.47  E-value: 6.42e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167234437   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950    1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 445-805 2.57e-26

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 109.73  E-value: 2.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 445 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 524
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 525 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 598
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 599 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 669
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 670 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 749
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167234437 750 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 805
Cdd:cd00200  238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
442-806 1.33e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.39  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 442 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 518
Cdd:COG2319   69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 519 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 596
Cdd:COG2319  146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 597 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 676
Cdd:COG2319  226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 677 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 756
Cdd:COG2319  302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 167234437 757 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 806
Cdd:COG2319  356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
328-694 1.21e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 107.30  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 328 SNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 405
Cdd:COG2319   97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 406 FLGNGDVL-TGDSGGVMLIWSktmvePPPGKGPkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnl 484
Cdd:COG2319  170 FSPDGKLLaSGSDDGTVRLWD-----LATGKLL-------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 485 ereievpdqygtiraVAEGRAEQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsV 564
Cdd:COG2319  233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-L 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 565 EHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIY 642
Cdd:COG2319  276 ATGELLRTLTGHSGgvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVR 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167234437 643 LYTvLENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIEN 694
Cdd:COG2319  356 LWD-LATGELLRTL---TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 398-691 8.32e-23

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 99.72  E-value: 8.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 398 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 476
Cdd:cd00200    9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELL------------RTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 477 LWD-HDLNLEREIEVPDQYgtIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 553
Cdd:cd00200   77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 554 QDRQVCMWNSVEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVD 628
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167234437 629 GTLLAVGSHDNFIYLYtvleNGRKYSRYGKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 691
Cdd:cd00200  231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
333-695 1.00e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 101.53  E-value: 1.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 333 LTVWDWQKKSKIAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKyekpkFVQCLAFLGNGDV 412
Cdd:COG2319   18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVLSVAFSPDGRL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 413 L-TGDSGGVMLIWSktmVEPPpgkgpkgvyQINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWD-HDLNLEREIEV 490
Cdd:COG2319   93 LaSASADGTVRLWD---LATG---------LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 491 PDqyGTIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsVEHRL 568
Cdd:COG2319  161 HS--GAVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 569 EWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTV 646
Cdd:COG2319  238 LLRTLTGHSGsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 167234437 647 lENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENG 695
Cdd:COG2319  318 -ATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362
WD40 COG2319
WD40 repeat [General function prediction only];
461-806 1.54e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.98  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 461 RNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQYGTIRAVAEGRAEQFLVGTSRNFILRGTFNDG-FQIEVQGHTDELWG 539
Cdd:COG2319    4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 540 LATHPFKDLLLTCAQDRQVCMWNsVEHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGN 617
Cdd:COG2319   84 VAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGavRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 618 EQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcK 697
Cdd:COG2319  163 GAVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-K 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 698 LIRnrsdckdidwttytcvlgfqvfgvwPEGSDGTDINALVRSHNRRVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSS 777
Cdd:COG2319  238 LLR-------------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSG 289

                        330       340
                 ....*....|....*....|....*....
gi 167234437 778 HVTNVSFTHNDSHLIStGGKDMSIIQWKL 806
Cdd:COG2319  290 GVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 245-598 1.36e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.09  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 245 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 325 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 401
Cdd:cd00200   70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 402 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 480
Cdd:cd00200  139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 481 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 560
Cdd:cd00200  207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 167234437 561 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 598
Cdd:cd00200  246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 9-64 1.64e-18

trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2.


Pssm-ID: 409268  Cd Length: 58  Bit Score: 80.15  E-value: 1.64e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167234437   9 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21947    2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNR 57
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 18-61 2.46e-16

trimerization domain of the echinoderm microtubule-associated protein-like family; The echinoderm microtubule-associated protein (EMAP)-like (EML) family includes EMAP-1, EMAP-2, EMAP-3, and EMAP-4. EMAP-1, also called EMAL1, EMAPL or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. EMAP-2, also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. EMAP-3, also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. EMAP-4, also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved trimerization domain located at the N-terminus of EML family members.


Pssm-ID: 409267  Cd Length: 44  Bit Score: 73.34  E-value: 2.46e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167234437  18 SDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVAS 61
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 236-562 6.07e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 79.30  E-value: 6.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 236 LFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiaGVDKDgrplqphVRVWDSVSLTTLHVigLGTFERGVGCLDFS 314
Cdd:cd00200   35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 315 KaDSGVHLCVIDDSNehmLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 392
Cdd:cd00200  103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 393 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGK 471
Cdd:cd00200  175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCL------------GTLRGHENGVNSVAFSPDGYLLASGSE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 472 DRKIILWDhdlnlereievpdqygtiravaegraeqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 551
Cdd:cd00200  240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278

                        330
                 ....*....|.
gi 167234437 552 CAQDRQVCMWN 562
Cdd:cd00200  279 GSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 19-64 1.78e-14

trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm microtubule-associated protein-like 2 (EMAP-2), also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. This model corresponds to the N-terminal trimerization domain of EMAP-2.


Pssm-ID: 409269  Cd Length: 48  Bit Score: 68.31  E-value: 1.78e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 167234437  19 DVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21948    2 EVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRK 47
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 580-806 2.50e-14

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 74.68  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 580 CADFHPSGTVVAIGTHSGRWFVLDAETRDLVS---IHTDGneqLSVMRYSVDGTLLAVGSHDNFIYLYTvLENGRKYSRY 656
Cdd:cd00200   14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP---VRDVAASADGTYLASGSSDKTIRLWD-LETGECVRTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 657 gkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcKLIRNRSDCKDidwttytcvlgfqvfgvwpegsdgtDINA 736
Cdd:cd00200   90 ---TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTD-------------------------WVNS 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 737 LVRSHNRRVIAVADDFCKVHLFQYPCSKakaPSHKYSAHSSHVTNVSFTHNDSHLISTGGkDMSIIQWKL 806
Cdd:cd00200  141 VAFSPDGTFVASSSQDGTIKLWDLRTGK---CVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
229-479 2.96e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.72  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 229 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 302
Cdd:COG2319  176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 303 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 380
Cdd:COG2319  244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 381 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 459
Cdd:COG2319  319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                        250       260
                 ....*....|....*....|
gi 167234437 460 MRNGMLLTGGGKDRKIILWD 479
Cdd:COG2319  381 SPDGRTLASGSADGTVRLWD 400
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 14-58 6.67e-12

trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.


Pssm-ID: 409270  Cd Length: 48  Bit Score: 60.81  E-value: 6.67e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 167234437  14 AASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDH 58
Cdd:cd21949    1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 660-806 1.28e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 660 TGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGCKLIRNrsdckdidwttytcvlgfqvfgvwpEGSDGTDINALVR 739
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-------------------------KGHTGPVRDVAAS 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167234437 740 SHNRRVIAVADDFCkVHLFQYpcsKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWKL 806
Cdd:cd00200   61 ADGTYLASGSSDKT-IRLWDL---ETGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDV 122
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 659-691 2.15e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.60  E-value: 2.15e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 167234437   659 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 691
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 569-689 1.94e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 40.04  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167234437 569 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSVDGTLLAVGSH-DNFIY 642
Cdd:COG0823   22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 167234437 643 LYTVLENGRKYSRYGKCTGHSSyithldWSPDNKHIM--SNSGDYEILY 689
Cdd:COG0823  101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLY 143
WD40 pfam00400
WD domain, G-beta repeat;
657-691 3.63e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 3.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 167234437  657 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 691
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 631-694 4.07e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.70  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167234437 631 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 694
Cdd:PTZ00420  89 ILASGSEDLTIRVWEIPHNDEsvKEIKDPQCilKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIEN 157
WD40 pfam00400
WD domain, G-beta repeat;
531-562 4.83e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 4.83e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 167234437  531 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 562
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 531-562 5.81e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 5.81e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 167234437   531 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 562
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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